BMRB Entry 6739

Name: Solution structure of SelM from Mus musculus
Published: 2005-12-28

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PDB ID: 2a2p
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6739
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of SelM from Mus musculus

Deposition date:

2005-07-21

Original release date:

2005-12-28

Authors:

Ferguson, A.; Labunskyy, V.; Fomenko, D.; Arac, D.; Chelliah, Y.; Amezcua, C.; Rizo, J.; Gladyshev, V.; Deisenhofer, J.

Citation:

Citation: Ferguson, A.; Labunskyy, V.; Fomenko, D.; Arac, D.; Chelliah, Y.; Amezcua, C.; Rizo, J.; Gladyshev, V.; Deisenhofer, J.. "NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of new thioredoxin-like family." J. Biol. Chem. ., .-. (2005).
PubMed: 16319061

Assembly members:

Assembly members:
Selenoprotein M, polymer, 129 residues, Formula weight is not available

Natural source:

Natural source: Common Name: House mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Selenoprotein M: MTNYRPDWNRLRGLARGRVE TCGGCQLNRLKEVKAFVTED IQLYHNLVMKHLPGADPELV LLSRNYQELERIPLSQMTRD EINALVQELGFYRKSAPEAQ VPPEYLWAPAKPPEEASEHD DLEHHHHHH

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
1H chemical shifts	874
13C chemical shifts	534
15N chemical shifts	123

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Selenoprotein M	1

Entities:

Entity 1, Selenoprotein M 129 residues - Formula weight is not available

1

MET

THR

ASN

TYR

ARG

PRO

ASP

TRP

ASN

ARG

2

LEU

ARG

GLY

LEU

ALA

ARG

GLY

ARG

VAL

GLU

3

THR

CYS

GLY

CYS

GLN

LEU

ASN

ARG

LEU

4

LYS

GLU

VAL

LYS

ALA

PHE

VAL

THR

GLU

ASP

5

ILE

GLN

LEU

TYR

HIS

ASN

LEU

VAL

MET

LYS

6

HIS

LEU

PRO

GLY

ALA

ASP

PRO

GLU

LEU

VAL

7

LEU

SER

ARG

ASN

TYR

GLN

GLU

LEU

GLU

8

ARG

ILE

PRO

LEU

SER

GLN

MET

THR

ARG

ASP

9

GLU

ILE

ASN

ALA

LEU

VAL

GLN

GLU

LEU

GLY

10

PHE

TYR

ARG

LYS

SER

ALA

PRO

GLU

ALA

GLN

11

VAL

PRO

GLU

TYR

LEU

TRP

ALA

PRO

ALA

12

LYS

PRO

GLU

ALA

SER

GLU

HIS

ASP

13

ASP

LEU

GLU

HIS

Samples:

sample_1: Selenoprotein M, [U-15N; U-13C], 1 mM; phosphate buffer 50 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 6; temperature: 298 K; ionic strength: 50 mM; pressure: 1 atm

Experiments:

Name	Sample	Sample state	Sample conditions
2D NOESY	sample_1	not available	sample_cond_1
2D TOCSY	sample_1	not available	sample_cond_1
3D 15N-separated NOESY	sample_1	not available	sample_cond_1
3D 13C-separated NOESY	sample_1	not available	sample_cond_1

Software:

VNMR v6.1C, Varian - collection

NMRPipe v1, Delaglio - processing

NMRView v5.2.2, Johnson - data analysis

ARIA v2.0, Nilges, M. - refinement, structure solution

NMR spectrometers:

Varian INOVA 600 MHz

REF	NP_444497
SWISS-PROT	Q8VHC3
GenBank	AAI47334 AAK95398 AAH19742 AAI47333
DBJ	BAE43252 BAE43327 BAC29028
PDB	2A2P